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Information on EC 4.2.1.144 - 3-amino-5-hydroxybenzoate synthase and Organism(s) Amycolatopsis mediterranei and UniProt Accession O52552

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.144 3-amino-5-hydroxybenzoate synthase
IUBMB Comments
A pyridoxal 5'-phosphate enzyme. The enzyme from the bacterium Amycolatopsis mediterranei participates in the pathway for rifamycin B biosynthesis. The enzyme also functions as a transaminase earlier in the pathway, producing UDP-alpha-D-kanosamine .
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This record set is specific for:
Amycolatopsis mediterranei
UNIPROT: O52552
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Word Map
The taxonomic range for the selected organisms is: Amycolatopsis mediterranei
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
ahba synthase, 3-amino-5-hydroxybenzoic acid synthase, 3-amino-5-hydroxybenzoate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-amino-5-hydroxybenzoic acid synthase
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AHBA synthase
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rifK
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SYSTEMATIC NAME
IUBMB Comments
5-amino-5-deoxy-3-dehydroshikimate hydro-lyase (3-amino-5-hydroxybenzoate-forming)
A pyridoxal 5'-phosphate enzyme. The enzyme from the bacterium Amycolatopsis mediterranei participates in the pathway for rifamycin B biosynthesis. The enzyme also functions as a transaminase earlier in the pathway, producing UDP-alpha-D-kanosamine [3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-amino-5-deoxy-3-dehydroshikimate
3-amino-5-hydroxybenzoate + H2O
show the reaction diagram
5-amino-5-deoxy-3-dehydroshikimate
3-amino-5-hydroxybenzoate + H2O
show the reaction diagram
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?
additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
gabaculine
crystal structure of the complex with enzyme
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-deoxy-D-arabinoheptulosonic acid 7-phosphate
1 mM, 40-50% activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.164
5-amino-5-deoxy-3-dehydroshikimate
pH 7.5, 28°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
195
pH 7.5, 28°C, recombinant enzyme
72
pH 7.5, 28°C, native enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28 - 50
more than 84% of maximum activity within
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
involved in rifamycin B biosynthesis. Starter enzyme for the assembly of the antibiotics' polyketide backbone
physiological function
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enzyme is part of the aminoshikimate pathway of formation of 3-amino-5-hydroxybenzoic acid, the precursor of ansamycin and other antibiotics. Nitrogenous precursor Kanosamine is phosphorylated and converted into 1-deoxy-1-imino-erythrose 4-phosphate, the substrate for the formation of 3,4-dideoxy-4-amino-D-arabino-seduheptulosonic acid 7-phosphate. This is converted via 5-deoxy-5-aminodehydroquinic acid and 5-deoxy-5-aminodehydroshikimic acid into 3-amino-5-hydroxybenzoic acid. 3-amino-5-hydroxybenzoic acid synthase seems to have two catalytic functions. As a homodimer, it catalyzes the last reaction in the pathway, the aromatization of 5-deoxy-5-aminodehydroshikimic acid, and at the beginning of the pathway in a complex with the oxidoreductase RifL it catalyzes the transamination of UDP-3-keto-D-glucose
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
2 * 39000, SDS-PAGE, 2 * 46101, calculated
46101
2 * 39000, SDS-PAGE, 2 * 46101, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with pyridoxal 5'-phosphate and with pyridoxal 5'-phosphate and inhibitor gabaculine. The overall fold of is similar to that of the aspartate aminotransferase family of PLP-dependent enzymes, with a large domain containing a seven-stranded beta-sheet surrounded by alpha-helices and a smaller domain consisting of a four-stranded antiparallel beta-sheet and four alpha-helices. The uninhibited form of the enzyme shows the cofactor covalently linked to residue Lys188 in an internal aldimine linkage. On binding the inhibitor, gabaculine, the internal aldimine linkage is broken, and a covalent bond is observed between the cofactor and inhibitor. The active site is composed of residues from two subunits, indicating that the enzyme is active as a dimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
both native and recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eads, J.C.; Beeby, M.; Scapin, G.; Yu, T.W.; Floss, H.G.
Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase
Biochemistry
38
9840-9849
1999
Amycolatopsis mediterranei (O52552), Amycolatopsis mediterranei, Amycolatopsis mediterranei S699 (O52552)
Manually annotated by BRENDA team
Floss, H.G.; Yu, T.W.; Arakawa, K.
The biosynthesis of 3-amino-5-hydroxybenzoic acid (AHBA), the precursor of mC7N units in ansamycin and mitomycin antibiotics: a review
J. Antibiot.
64
35-44
2011
Amycolatopsis mediterranei
Manually annotated by BRENDA team
Kim, C.G.; Yu, T.W.; Fryhle, C.B.; Handa, S.; Floss, H.G.
3-Amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics
J. Biol. Chem.
273
6030-6040
1998
Amycolatopsis mediterranei (O52552), Amycolatopsis mediterranei
Manually annotated by BRENDA team